ID A0A2A4GA21_9FLAO Unreviewed; 1503 AA.
AC A0A2A4GA21;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:PCE64602.1};
GN ORFNames=B7P33_10015 {ECO:0000313|EMBL:PCE64602.1};
OS Sediminicola luteus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=319238 {ECO:0000313|EMBL:PCE64602.1, ECO:0000313|Proteomes:UP000219559};
RN [1] {ECO:0000313|EMBL:PCE64602.1, ECO:0000313|Proteomes:UP000219559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HQA918 {ECO:0000313|EMBL:PCE64602.1,
RC ECO:0000313|Proteomes:UP000219559};
RA Chen L.;
RT "A new member of the family Flavobacteriaceae isolated from ascidians.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCE64602.1}.
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DR EMBL; NBWU01000003; PCE64602.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000219559; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000219559}.
FT DOMAIN 18..412
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 899..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1503 AA; 166699 MW; AE94EF63DCD3BE71 CRC64;
MGKHAQGLYL PEFEHENCGA GFICNLNGEK SNQIIHDALE ILVKLEHRGG VSSDGKTGDG
AGLMIDIPHE YFTRVCGFEL PEQRKYAVGM VFLPKSPNQY SFCKAEFEKE LKTQGLTVLG
WRKVPVDPSH LGEIALASEP NIEQVFVAQG ELEEHIFKAR LYAARKIAEH AIRLSKISEA
DAFYVSSLSN TTLIYKGIIM PEDIGPYFLD LQQPDLVTRM ALVHQRFSTN TMPTWELAQP
FRFLCQNGEI NTLRGNVSRM RVREEIMKSD IFGDQIERLF PIILPGKSDS ASMDMSVELL
TLTGRSLPEV MMMTIPEAWE RHATMSEDRK AFYEYNSCIM EPWDGPASVP FADGDYIGAL
LDRNGLRPSR YTVTKSGKLI MSSEVGVVDL DPADIESHGR LEPGKMFLVD MNEGRIVGDE
EIKDKIVTQR PYKKWLNENN LQLKDVPNNN TACPIETLDL NTRQRLYNYT IEDIQEVIVP
MAQNGKEALG SMGIDTPLAV LSDRPQLIPN YFKQLFAQVT NPPLDGIREE VVTDISLALG
HDKNIFEIIP EQCNKLRIQN PVISNNDLEK IRNIDVNGFK AETIAILYDK NKGVNGLEDA
LDQIIIQITK ALDQGVNIII LSDRGAKKGS APIPALLACS YVHHQMNRLR KRSYFDIVIE
SAEPREPHHF ATLFGYGASA INPYMVNEII RLQVEEGFIA LDAQKAVDNF NKAIGKGILK
VMNKIGISTL HSYRGSQIFE IVGFNSAFVE KYFPYTASRI EGIGLYEIEK EIHKRYEYAY
PERHIDKRLG LNIGGEYRWR RNGERHLFNP TTVAKLQQSV RLNDQNAYDT YKDAINEQAK
NLLTLRGLFE FDNLDPIPLE EVEPWTEIVK RFKTGAMSYG SISREAHENL AIAMNRLGAK
SNSGEGGEDR RRFQPAPNGD NKNSAIKQVA SGRFGVTSHY LSSAQEIQIK MAQGAKPGEG
GQLPGHKVLP WIADARNSTP FVGLVSPPPH HDIYSIEDLA QLIYDLKNAN REARINVKLV
SEVGVGTIAA GVAKAKADVV LISGYDGGTG ASPLTSLKHA GLPWELGLAE AQQTLVMNNL
RSRIVVECDG QLKTGRDVAV AALLGAEEFG FATAPLVASG CIMMRKCHLN TCPVGIATQD
KELRKNFKGT PEHVINFFYY VANELRQIMA QLGFRTVDEM VGQTQKLNTN KAIQHYKAKG
LDLSSILYQP ANYNEFTIRN TETQDHNLDN VMDFRILKDG HAAIFRKEPT HLAYDIHNTD
RSLGAIVSNE ISKIYGHLGL PEDTLNLSFK GSAGQSFGVF GAAGITYTIE GNTNDYLGKG
LSGAKIIVKK PADADFVAED NIIVGNVCLF GGVKGEAYIN GIAGERFAVR NSGVTAVVEG
VGDHGCEYMT GGRIVVLGKT GRNFAAGMSG GYAYVLNQSG QFTDGLCNEE TVDFDPITEA
DAAELKALIS NHLNYTDSKR AAEILADWDS YLAKFVKVMP KEYKVALERI ANEEPMVEEL
TVA
//
